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Biocell

versión impresa ISSN 0327-9545

Biocell vol.36 no.3 Mendoza dic. 2012

 

ORIGINAL ARTICLES

A likely role for a novel PH-domain containing protein, PEPP2, in connecting membrane and cytoskeleton

 

Yi Zou and Wenping Zhong

Department of Biology, School of Life Science and Technology, Jinan University, Guangzhou, China

 

Address correspondence to:

Yi Zou.
Department of Biology, School of Life Science and Technology, Jinan University, Guangzhou 510632, R.P. China. E-mail: tyizou@jnu.edu.cn

 


ABSTRACT:  PH domains (pleckstrin homology) are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular apartments with assistances of alternative binding partners. PH domain-containing proteins are found to be involved in a wide range of cellular events, including signalling, cytoskeleton rearrangement and vesicular trafficking. Here we showed that a novel PH domain-containing protein, PEPP2, displayed moderate phosphoinositide binding specificity. Full length PEPP2 associated with both plasma membrane and microtubules. The membrane-associated PEPP2 nucleated at cell-cell contacts and the leading edge of migrating cells. Overexpression of PEPP2 increased membrane microviscosity, indicating a potential role of PEPP2 in regulating function of membrane and microtubules.

Key words: Microtubule; Membrane; Phosphoinositide; Microviscosity; Wortmannin


 

El texto del artículo fue retirado el 5 de Mayo de 2014 a solicitud del editor.

The text of this article was removed on May, 5th by request of the chief editor. 

 

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Received: April 13, 2012.
Revised version received: August 7, 2012.
Accepted: October 10, 2012.

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